Zobrazeno 1 - 10
of 135
pro vyhledávání: '"Leonard J. Banaszak"'
Autor:
Amy J. Reese, Leonard J. Banaszak
Publikováno v:
Journal of Lipid Research, Vol 45, Iss 2, Pp 232-243 (2004)
The family of proteins accountable for the intracellular movement of lipids is characterized by a 10-stranded β-barrel that forms an internalized cavity varying in size and binding preferences. The loop connecting β-strands E and F (the fifth and s
Externí odkaz:
https://doaj.org/article/45bc930c1d074212a042afef1e554c2b
Autor:
Leonard J. Banaszak
Imagine trying to understand an engine without visualizing its moving parts. Biological processes involve far more complex chemical reactions and components than any engine. Furthermore, the parts work together to do many more functions than an engin
Autor:
Ulrich Brandt, Abir L. Banerjee, Paul P. Van Veldhoven, D. K. Srivastava, Peter J. Hanley, Stefan Dröse, Jtirgen Daut, Joseph J. Barycki, Leonard J. Banaszak, Rachel A. Lareau
Publikováno v:
The Journal of Physiology. 562:307-318
5-Hydroxydecanoate (5-HD) blocks pharmacological and ischaemic preconditioning, and has been postulated to be a specific inhibitor of mitochondrial ATP-sensitive K+ (KATP) channels. However, recent work has shown that 5-HD is activated to 5-hydroxyde
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::868f893e2a08208a5b09535a940e01cc
https://doi.org/10.1113/jphysiol.2004.073932
https://doi.org/10.1113/jphysiol.2004.073932
Autor:
Leonard J. Banaszak, Amy J. Reese
Publikováno v:
Journal of Lipid Research, Vol 45, Iss 2, Pp 232-243 (2004)
The family of proteins accountable for the intracellular movement of lipids is characterized by a 10-stranded beta-barrel that forms an internalized cavity varying in size and binding preferences. The loop connecting beta-strands E and F (the fifth a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1b9ec66659da89e1d25788fad8b411b2
https://doi.org/10.1194/jlr.m300113-jlr200
https://doi.org/10.1194/jlr.m300113-jlr200
Publikováno v:
European Journal of Biochemistry. 269:4176-4184
Escherichia coli 3-phosphoglycerate dehydrogenase (PGDH) catalyzes the first step in serine biosynthesis, and is allosterically inhibited by serine. Structural studies revealed a homotetramer in which the quaternary arrangement of subunits formed an
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b673cf1857ad006dfeab79cb4fa8c906
https://doi.org/10.1046/j.1432-1033.2002.03075.x
https://doi.org/10.1046/j.1432-1033.2002.03075.x
Autor:
James R. Thompson, Leonard J. Banaszak
Publikováno v:
Biochemistry. 41:9398-9409
The refined molecular structure of lipovitellin is described using synchrotron cryocrystallographic data to 1.9 A resolution. Lipovitellin is the predominant lipoprotein found in the yolk of egg-laying animals and is involved in lipid and metal stora
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::162fed8bea416505a170b61063dd79e2
https://doi.org/10.1021/bi025674w
https://doi.org/10.1021/bi025674w
Publikováno v:
Protein Engineering, Design and Selection. 15:603-610
Two artificial transaminases were assembled by linking a pyridoxamine derivative within an engineered fatty acid binding protein. The goal of mimicking a native transamination site by stabilizing a cationic pyridoxamine ring system was approached usi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0d5fdac4eebc7d279371a9f64e244bb6
https://doi.org/10.1093/protein/15.7.603
https://doi.org/10.1093/protein/15.7.603
Publikováno v:
Protein Science. 11:1552-1557
Fumarase catalyzes the reversible conversion of fumarate to S- malate during the operation of the ubiquitous Kreb's cycle. Previous studies have shown that the active site includes side chains from three of the four subunits within the tetrameric enz
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::821db193e1cee637d6e45f81220e3512
https://doi.org/10.1110/ps.0201502
https://doi.org/10.1110/ps.0201502
Publikováno v:
Journal of Biological Chemistry. 277:7567-7573
In Escherichia coli, the homodimeric Krebs cycle enzyme isocitrate dehydrogenase (EcIDH) is regulated by reversible phosphorylation of a sequestered active site serine. The phosphorylation cycle is catalyzed by a bifunctional protein, IDH kinase/phos
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f77320bab5239cdab96937ce564b9979
https://doi.org/10.1074/jbc.m107908200
https://doi.org/10.1074/jbc.m107908200
Publikováno v:
Selected Papers of Michael G Rossmann with Commentaries ISBN: 9789814513340
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7c0fc55d8e4ec5e9b437017373477c0f
https://doi.org/10.1142/9789814513357_0012
https://doi.org/10.1142/9789814513357_0012